Penicillin amidase from Proteus rettgeri.
1. Penicillin amidase from Proteus rettgeri was purified 580-fold by a four-step chromatographic procedure. Titration with phenylmethanesulphonyl fluoride showed that the purified preparation contains 53% of the enzyme. 2. The molecular weight of the amidase was found to be 65.000. The enzyme is strongly inhibited by N-bromosuccinimide and zinc ions. It hydrolyses penicillins, cephalosporins and some synthetic substrates, and in addition it catalyses synthesis of ampicillin from methyl ester of phenylglycine and 6-aminopenicillanic acid. 3. The immobilized amidase obtained by copolymerization of the chemically modified enzyme with acrylamide was applied for preparative hydrolysis of benzylpenicillin.
D000581:Amidohydrolases / Q000302:isolation & purification*; D001419:Bacteria / Q000201:enzymology; D008670:Metals / Q000494:pharmacology; D008970:Molecular Weight; D010399:Penicillin Amidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D010400:Penicillin G / Q000378:metabolism; D010404:Penicillin V / Q000378:metabolism; D011511:Proteus / Q000201:enzymology*; D013379:Substrate Specificity; D013997:Time Factors
D008670:Metals; D000581:Amidohydrolases; D010399:Penicillin Amidase; D010400:Penicillin G; D010404:Penicillin V